ID ORC5_HUMAN Reviewed; 435 AA. AC O43913; A4D0P8; O60590; O95268; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 02-SEP-2026, entry version 192. DE RecName: Full=Origin recognition complex subunit 5; GN Name=ORC5; Synonyms=ORC5L; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9829972; DOI=10.1074/jbc.273.49.32421; RA Tugal T., Zou-Yang X.H., Gavin K., Pappin D., Canas B., Kobayashi R., RA Hunt T., Stillman B.; RT "The Orc4p and Orc5p subunits of the Xenopus and human origin recognition RT complex are related to Orc1p and Cdc6p."; RL J. Biol. Chem. 273:32421-32429(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9417919; DOI=10.1006/geno.1997.5003; RA Ishiai M., Dean F.B., Okumura K., Abe M., Moon K.-Y., Amin A.A., RA Kagotani K., Taguchi H., Murakami Y., Hanaoka F., O'Donnell M., Hurwitz J., RA Eki T.; RT "Isolation of human and fission yeast homologues of the budding yeast RT origin recognition complex subunit ORC5: human homologue (ORC5L) maps to RT 7q22."; RL Genomics 46:294-298(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, TISSUE RP SPECIFICITY, AND VARIANT ARG-37. RX PubMed=9765232; DOI=10.1074/jbc.273.42.27137; RA Quintana D.G., Thome K.C., Hou Z.-H., Ligon A.H., Morton C.C., Dutta A.; RT "ORC5L, a new member of the human origin recognition complex, is deleted in RT uterine leiomyomas and malignant myeloid diseases."; RL J. Biol. Chem. 273:27137-27145(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP IDENTIFICATION IN THE ORC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND RP ASSEMBLY OF THE ORC COMPLEX. RX PubMed=12909626; DOI=10.1074/jbc.m307535200; RA Ohta S., Tatsumi Y., Fujita M., Tsurimoto T., Obuse C.; RT "The ORC1 cycle in human cells: II. Dynamic changes in the human ORC RT complex during the cell cycle."; RL J. Biol. Chem. 278:41535-41540(2003). RN [9] RP RECONSTITUTION OF THE ORC COMPLEX, AND DISASSEMBLY OF THE ORC COMPLEX. RX PubMed=17716973; DOI=10.1074/jbc.m705905200; RA Siddiqui K., Stillman B.; RT "ATP-dependent assembly of the human origin recognition complex."; RL J. Biol. Chem. 282:32370-32383(2007). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP FUNCTION, UBIQUITINATION, AND SUBCELLULAR LOCATION. RX PubMed=31160578; DOI=10.1038/s41467-019-10321-x; RA Coulombe P., Nassar J., Peiffer I., Stanojcic S., Sterkers Y., RA Delamarre A., Bocquet S., Mechali M.; RT "The ORC ubiquitin ligase OBI1 promotes DNA replication origin firing."; RL Nat. Commun. 10:2426-2426(2019). CC -!- FUNCTION: Component of the origin recognition complex (ORC) that binds CC origins of replication. DNA-binding is ATP-dependent. The specific DNA CC sequences that define origins of replication have not been identified CC yet. ORC is required to assemble the pre-replication complex necessary CC to initiate DNA replication. {ECO:0000269|PubMed:31160578}. CC -!- SUBUNIT: Component of ORC, a complex composed of at least 6 subunits: CC ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle CC dependent manner. It is sequentially assembled at the exit from CC anaphase of mitosis and disassembled as cells enter S phase. CC {ECO:0000269|PubMed:12909626}. CC -!- INTERACTION: CC O43913; Q13415: ORC1; NbExp=11; IntAct=EBI-374928, EBI-374847; CC O43913; Q13416: ORC2; NbExp=15; IntAct=EBI-374928, EBI-374957; CC O43913; Q9UBD5: ORC3; NbExp=15; IntAct=EBI-374928, EBI-374916; CC O43913; O43929: ORC4; NbExp=2; IntAct=EBI-374928, EBI-374889; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31160578}. Chromosome CC {ECO:0000269|PubMed:31160578}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O43913-1; Sequence=Displayed; CC Name=2; Synonyms=ORC5T; CC IsoId=O43913-2; Sequence=VSP_042037; CC -!- TISSUE SPECIFICITY: Abundant in spleen, ovary, prostate, testis, and CC colon mucosa. {ECO:0000269|PubMed:9765232}. CC -!- PTM: Multi-mono-ubiquitinated by OBI1; ubiquitination is important for CC efficient DNA replication origin site activation. Ubiquitination levels CC are low in mitotic and early G1-phAse cells and are induced in late CC G1-/early S-phase, peaking in S-phase and decrease toward the end of CC the cell cycle. {ECO:0000269|PubMed:31160578}. CC -!- MISCELLANEOUS: [Isoform 2]: Does not interact with ORC2. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ORC5 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF047599; AAC80283.1; -; mRNA. DR EMBL; U92538; AAC51933.1; -; mRNA. DR EMBL; AF049127; AAC63972.1; -; mRNA. DR EMBL; AF081459; AAC64401.1; -; mRNA. DR EMBL; AC002067; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007393; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH236947; EAL24409.1; -; Genomic_DNA. DR EMBL; CH471070; EAW83341.1; -; Genomic_DNA. DR EMBL; BC023652; AAH23652.1; -; mRNA. DR CCDS; CCDS47681.1; -. [O43913-2] DR CCDS; CCDS5734.1; -. [O43913-1] DR RefSeq; NP_002544.1; NM_002553.4. [O43913-1] DR RefSeq; NP_859531.1; NM_181747.4. [O43913-2] DR PDB; 5UJ7; X-ray; 3.39 A; E/F=1-284. DR PDB; 5UJM; EM; 18.00 A; E=1-435. DR PDB; 7CTE; EM; 3.80 A; E=1-435. DR PDB; 7CTF; EM; 4.80 A; E=1-435. DR PDB; 7CTG; EM; 5.00 A; E=1-435. DR PDB; 7JPO; EM; 3.20 A; E=1-435. DR PDB; 7JPP; EM; 3.70 A; E=1-435. DR PDB; 7JPQ; EM; 3.50 A; E=1-435. DR PDB; 7JPR; EM; 4.00 A; E=1-435. DR PDB; 7JPS; EM; 4.40 A; E=1-435. DR PDB; 8RWV; EM; 6.68 A; E=1-435. DR PDB; 8S0C; EM; 4.00 A; E=1-435. DR PDB; 8S0D; EM; 3.60 A; E=1-435. DR PDB; 8S0E; EM; 3.80 A; E=1-435. DR PDB; 8S0F; EM; 4.10 A; E=1-435. DR AlphaFoldDB; O43913; -. DR EMDB; EMD-19566; -. DR EMDB; EMD-19621; -. DR EMDB; EMD-19622; -. DR EMDB; EMD-19623; -. DR EMDB; EMD-19624; -. DR EMDB; EMD-22417; -. DR EMDB; EMD-22418; -. DR EMDB; EMD-22419; -. DR EMDB; EMD-22420; -. DR EMDB; EMD-22421; -. DR EMDB; EMD-30462; -. DR EMDB; EMD-30463; -. DR EMDB; EMD-30464; -. DR SMR; O43913; -. DR BioGRID; 111043; 96. DR ComplexPortal; CPX-1880; Nuclear origin recognition complex. DR CORUM; O43913; -. DR DIP; DIP-29691N; -. DR FunCoup; O43913; 4358. DR IntAct; O43913; 63. DR MINT; O43913; -. DR NDEx; IQUERY-CP-ORC5; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000297431; -. DR BindingDB; O43913; -. DR ChEMBL; CHEMBL5725187; -. DR GlyGen; O43913; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O43913; -. DR PhosphoSitePlus; O43913; -. DR SwissPalm; O43913; -. DR BioMuta; ORC5; -. DR jPOST; O43913; -. DR MassIVE; O43913; -. DR PaxDb; 9606-ENSP00000297431; -. DR PeptideAtlas; O43913; -. DR ProteomicsDB; 49227; -. [O43913-1] DR ProteomicsDB; 49228; -. [O43913-2] DR Pumba; O43913; -. DR Antibodypedia; 31233; 93 antibodies from 25 providers. DR DNASU; 5001; -. DR Ensembl; ENST00000297431.9; ENSP00000297431.4; ENSG00000164815.12. [O43913-1] DR Ensembl; ENST00000447452.6; ENSP00000395747.2; ENSG00000164815.12. [O43913-2] DR GeneID; 5001; -. DR KEGG; hsa:5001; -. DR MANE-Select; ENST00000297431.9; ENSP00000297431.4; NM_002553.4; NP_002544.1. DR UCSC; uc003vcb.3; human. [O43913-1] DR AGR; HGNC:8491; -. DR ClinPGx; PA32812; -. DR CTD; 5001; -. DR DisGeNET; 5001; -. DR GeneCards; ORC5; -. DR HGNC; HGNC:8491; ORC5. DR HPA; ENSG00000164815; Low tissue specificity. DR MIM; 602331; gene. DR OpenTargets; ENSG00000164815; -. DR VEuPathDB; HostDB:ENSG00000164815; -. DR eggNOG; KOG2543; Eukaryota. DR GeneTree; ENSGT00390000009380; -. DR HOGENOM; CLU_028223_0_0_1; -. DR InParanoid; O43913; -. DR OMA; QLRRWHG; -. DR OrthoDB; 365981at2759; -. DR PAN-GO; O43913; 3 GO annotations based on evolutionary models. DR PhylomeDB; O43913; -. DR BRENDA; 3.6.4.B8; 2681. DR PathwayCommons; O43913; -. DR Reactome; R-HSA-113507; E2F-enabled inhibition of pre-replication complex formation. DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress. DR Reactome; R-HSA-68616; Assembly of the ORC complex at the origin of replication. DR Reactome; R-HSA-68689; CDC6 association with the ORC:origin complex. DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex. DR Reactome; R-HSA-68949; Orc1 removal from chromatin. DR Reactome; R-HSA-68962; Activation of the pre-replicative complex. DR SignaLink; O43913; -. DR SIGNOR; O43913; -. DR Agora; ENSG00000164815; -. DR BioGRID-ORCS; 5001; 462 hits in 1183 CRISPR screens. DR ChiTaRS; ORC5; human. DR GeneWiki; ORC5; -. DR GeneWiki; ORC5L; -. DR GenomeRNAi; 5001; -. DR Pharos; O43913; Tbio. DR PRO; PR:O43913; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; O43913; protein. DR Bgee; ENSG00000164815; Expressed in secondary oocyte and 195 other cell types or tissues. DR ExpressionAtlas; O43913; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0005694; C:chromosome; EXP:UniProtKB. DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL. DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0000808; C:origin recognition complex; IDA:UniProtKB. DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central. DR GO; GO:0000166; F:nucleotide binding; TAS:ProtInc. DR GO; GO:0006260; P:DNA replication; NAS:UniProtKB. DR GO; GO:0006270; P:DNA replication initiation; IDA:ComplexPortal. DR GO; GO:0006275; P:regulation of DNA replication; IDA:UniProtKB. DR FunFam; 3.40.50.300:FF:000673; Origin recognition complex subunit 5; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR041664; AAA_16. DR InterPro; IPR020796; ORC5. DR InterPro; IPR047088; ORC5_C. DR InterPro; IPR048866; ORC5_lid. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR12705; ORIGIN RECOGNITION COMPLEX SUBUNIT 5; 1. DR PANTHER; PTHR12705:SF0; ORIGIN RECOGNITION COMPLEX SUBUNIT 5; 1. DR Pfam; PF13191; AAA_16; 1. DR Pfam; PF14630; ORC5_C; 1. DR Pfam; PF21639; ORC5_lid; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PDBsum; 5UJ7; -. DR PDBsum; 5UJM; -. DR PDBsum; 7CTE; -. DR PDBsum; 7CTF; -. DR PDBsum; 7CTG; -. DR PDBsum; 7JPO; -. DR PDBsum; 7JPP; -. DR PDBsum; 7JPQ; -. DR PDBsum; 7JPR; -. DR PDBsum; 7JPS; -. DR PDBsum; 8RWV; -. DR PDBsum; 8S0C; -. DR PDBsum; 8S0D; -. DR PDBsum; 8S0E; -. DR PDBsum; 8S0F; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Chromosome; KW DNA replication; Nucleotide-binding; Nucleus; Proteomics identification; KW Reference proteome; Ubl conjugation. FT CHAIN 1..435 FT /note="Origin recognition complex subunit 5" FT /id="PRO_0000127092" FT BINDING 37..44 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT VAR_SEQ 294..435 FT /note="LSAHTHVELPYYSKFILIAAYLASYNPARTDKRFFLKHHGKIKKTNFLKKHE FT KTSNHLLGPKPFPLDRLLAILYSIVDSRVAPTANIFSQITSLVTLQLLTLVGHDDQLDG FT PKYKCTVSLDFIRAIARTVNFDIIKYLYDFL -> IRGSIETVTGDTSSANYQDTKVNT FT KEHSVRK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9765232" FT /id="VSP_042037" FT VARIANT 37 FT /note="G -> R (in dbSNP:rs1056677)" FT /evidence="ECO:0000269|PubMed:9765232" FT /id="VAR_011800" FT VARIANT 52 FT /note="K -> N (in dbSNP:rs2307413)" FT /id="VAR_014524" FT VARIANT 166 FT /note="R -> C (in dbSNP:rs2307402)" FT /id="VAR_014525" FT HELIX 13..22 FT /evidence="ECO:0007829|PDB:7JPO" FT STRAND 24..27 FT /evidence="ECO:0007829|PDB:7JPO" FT STRAND 31..36 FT /evidence="ECO:0007829|PDB:7JPO" FT STRAND 39..42 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 43..53 FT /evidence="ECO:0007829|PDB:7JPO" FT STRAND 58..62 FT /evidence="ECO:0007829|PDB:7JPO" FT TURN 63..65 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 69..84 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 99..110 FT /evidence="ECO:0007829|PDB:7JPO" FT STRAND 115..118 FT /evidence="ECO:0007829|PDB:7JPO" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:7JPO" FT TURN 131..133 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 137..142 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 144..148 FT /evidence="ECO:0007829|PDB:7JPO" FT STRAND 152..160 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:7JPO" FT STRAND 175..178 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 180..182 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 184..191 FT /evidence="ECO:0007829|PDB:7JPO" FT TURN 192..194 FT /evidence="ECO:0007829|PDB:5UJ7" FT HELIX 201..215 FT /evidence="ECO:0007829|PDB:7JPO" FT TURN 216..218 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 222..236 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 238..242 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 250..267 FT /evidence="ECO:0007829|PDB:7JPO" FT TURN 268..271 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 275..283 FT /evidence="ECO:0007829|PDB:7JPO" FT STRAND 294..296 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 304..317 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 321..323 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 325..329 FT /evidence="ECO:0007829|PDB:7JPO" FT TURN 350..352 FT /evidence="ECO:0007829|PDB:7JPQ" FT HELIX 359..369 FT /evidence="ECO:0007829|PDB:7JPO" FT STRAND 370..372 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 378..389 FT /evidence="ECO:0007829|PDB:7JPO" FT STRAND 392..395 FT /evidence="ECO:0007829|PDB:7JPO" FT STRAND 401..403 FT /evidence="ECO:0007829|PDB:7JPO" FT STRAND 407..409 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 413..422 FT /evidence="ECO:0007829|PDB:7JPO" FT HELIX 428..431 FT /evidence="ECO:0007829|PDB:7JPO" SQ SEQUENCE 435 AA; 50283 MW; 0FEB0E829C124745 CRC64; MPHLENVVLC RESQVSILQS LFGERHHFSF PSIFIYGHTA SGKTYVTQTL LKTLELPHVF VNCVECFTLR LLLEQILNKL NHLSSSEDGC STEITCETFN DFVRLFKQVT TAENLKDQTV YIVLDKAEYL RDMEANLLPG FLRLQELADR NVTVLFLSEI VWEKFRPNTG CFEPFVLYFP DYSIGNLQKI LSHDHPPEYS ADFYAAYINI LLGVFYTVCR DLKELRHLAV LNFPKYCEPV VKGEASERDT RKLWRNIEPH LKKAMQTVYL REISSSQWEK LQKDDTDPGQ LKGLSAHTHV ELPYYSKFIL IAAYLASYNP ARTDKRFFLK HHGKIKKTNF LKKHEKTSNH LLGPKPFPLD RLLAILYSIV DSRVAPTANI FSQITSLVTL QLLTLVGHDD QLDGPKYKCT VSLDFIRAIA RTVNFDIIKY LYDFL //